To explore the interaction of benzenehexacarboxylate with mutant hemoglobins like hemoglobin S (beta6 Glu-Val) and hemoglobin C (beta6 Glu-Lys), with the deoxy form of the isolated beta subunits of hemoglobin A and with the liganded and unliganded form of the isolated beta subunits of hemoglobin S. To measure the sedimentation behavior of partially ligated solutions of normal hemoglobin. At present we are standardizing the use of a monochromator accessory with the absorption optics of the analytical ultracentrifuge. To explore the conformation in solution normal and mutant apohemoglobins, their interaction with polyanions and their recombination with the heme, both in the presence and absence of polyanions.